Open AccessLigand kinetics of hemoglobin S containing erythrocytes.
Author(s) -
John P. Harrington,
Danek Elbaum,
Robert M. Bookchin,
Jonathan B. Wittenberg,
Ronald L. Nagel
Publication year - 1977
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.74.1.203
Subject(s) - oxygenation , hemoglobin , red cell , extracellular , chemistry , intracellular , oxygen , kinetics , biophysics , ligand (biochemistry) , biochemistry , red blood cell , biology , receptor , medicine , physics , organic chemistry , quantum mechanics , ecology
Oxygen uptake of fully deoxygenated sickle (SS) erythrocytes is slower than that of normal (AA) erythrocytes, as demonstrated by the half-times of the overall oxygenation reactions: at 25 degrees in an isotonic phosphate buffer the normal red cells have a t1/2 = 82 +/- 4.7 msec, as compared to sickle red cells where t1/2 = 135 +/- 17.6 msec. The effects of temperature, extracellular osmolality, and the presence of an antisickling agent (n-butylurea) on the rate of red cell oxygenation strongly suggest that the differences in oxygenation rates encountered with sickle red cells is directly related to the intracellular polymerization of deoxyhemoglobin S.